{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,28]],"date-time":"2026-08-28T00:24:17Z","timestamp":1787876657222,"version":"build-2784847793"},"reference-count":43,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2013,2,18]],"date-time":"2013-02-18T00:00:00Z","timestamp":1361145600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Cellular Biochemistry"],"published-print":{"date-parts":[[2013,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>SPINKL, a serine protease inhibitor kazal\u2010type\u2010like protein initially found in mouse seminal vesicle secretions, possesses structurally conserved six\u2010cysteine residues of the kazal\u2010type serine protease inhibitor family. However, it has no inhibitory activity against serine proteases. Previously, it was found to have the ability to suppress murine sperm capacitation in vitro. Herein, we investigated the mechanisms underlying the suppressive effect of SPINKL on sperm capacitation. Three in vitro capacitation\u2010enhancing agents, including bovine serum albumin (BSA), methyl\u2010beta\u2010cyclodextrin (MBCD), and dibutyryl cyclic AMP (dbcAMP), coupled with 3\u2010isobutyl\u20101\u2010methylxanthine (IBMX), were used to evaluate the influence of SPINKL on capacitation signaling. Preincubation of sperm with SPINKL suppressed BSA\u2010 and MBCD\u2010induced sperm capacitation by blocking three upstream signals of capacitation that is the cholesterol efflux from sperm plasma membranes, extracellular calcium ion influx into sperm, and increases in intracellular cAMP. Moreover, SPINKL also inhibited downstream signal transduction of capacitation since it suppressed dbcAMP\/IBMX and N<jats:sup>6<\/jats:sup>\u2010phenyl cAMP (6\u2010Phe\u2010cAMP)\u2010activated cAMP\u2010dependent protein kinase\u2010associated protein tyrosine phosphorylation. Such inhibition is probably mediated by attenuation of SRC tyrosine kinase activity. Furthermore, SPINKL could not reverse capacitation once sperm had been capacitated by capacitation\u2010enhancing agents or capacitated in vivo in the oviduct. SPINKL bound to sperm existed in the uterus but had disappeared from sperm in the oviduct during the sperm's transit through the female reproductive tract. Therefore, SPINKL may serve as an uncapacitation factor in the uterus to prevent sperm from precocious capacitation and the subsequent acrosome reaction and thus preserve the fertilization ability of sperm. J. Cell. Biochem. 114: 888\u2013898, 2013. \u00a9 2012 Wiley Periodicals, Inc.<\/jats:p>","DOI":"10.1002\/jcb.24428","type":"journal-article","created":{"date-parts":[[2012,10,23]],"date-time":"2012-10-23T17:17:48Z","timestamp":1351012668000},"page":"888-898","source":"Crossref","is-referenced-by-count":29,"title":["Mechanisms underlying the inhibition of murine sperm capacitation by the seminal protein, SPINKL"],"prefix":"10.1002","volume":"114","author":[{"given":"Huan\u2010Chin","family":"Tseng","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert 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